ID   MURD_BARQU              Reviewed;         466 AA.
AC   Q6G122;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE            EC=6.3.2.9;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
DE   AltName: Full=D-glutamic acid-adding enzyme;
GN   Name=murD; OrderedLocusNames=BQ08880;
OS   Bartonella quintana (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine +
CC       glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; BX897700; CAF26367.1; -; Genomic_DNA.
DR   RefSeq; YP_032500.1; -.
DR   GeneID; 2867307; -.
DR   GenomeReviews; BX897700_GR; BQ08880.
DR   KEGG; bqu:BQ08880; -.
DR   NMPDR; fig|283165.1.peg.770; -.
DR   HOGENOM; Q6G122; -.
DR   OMA; Q6G122; SEDHLDR.
DR   BioCyc; BQUI283165:BQ08880-MON; -.
DR   BRENDA; 6.3.2.9; 292235.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate lig...; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00639; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    466       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000108972.
FT   NP_BIND     128    134       ATP (Potential).
SQ   SEQUENCE   466 AA;  51034 MW;  E02078B4F6E24915 CRC64;
     MISCTCYKGQ KVALFGLGKS GLAAAQALMS GGAKVVAWDD NPSGVHTAKR ENIPTRDLQY
     ENWSEFVALI LAPGVPLTYP QPHWVVDKAR QADIEIVGDI ELFVRARNHF LQHSGFRDQD
     VPFIAITGTN GKSTTTALLA HLLEQMGYDV QMGGNIGTAI LTLKPFVKKR IYVIECSSFQ
     IELTPSLQPT IGLLLNLTSD HIDRHGSFAA YVQAKRRLVT GASYAFISVD NAVCQALYQQ
     LLDEGHQVGA VSKEHFVENG FYADRTKLFS VCQGQRHMLA DLADMTALRG SHNAQNALMV
     LATLQALKIS DPHIEKYLAS YKGLAHRMQQ VRKMGPVLFI NDSKATNAEA SAPALSTFND
     IFWIVGGQAK EGGIEALRGF FHKIRKAYLI GEAAQEFAGV IGSAFPFSMS LTLENAVHEA
     TVDAMCCKAK EAVVLFSPAC ASYDQFKNYE VRGEAFVSFV MQLKES
//